| pubmed-article:17517630 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17517630 | lifeskim:mentions | umls-concept:C0345904 | lld:lifeskim |
| pubmed-article:17517630 | lifeskim:mentions | umls-concept:C0061928 | lld:lifeskim |
| pubmed-article:17517630 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:17517630 | lifeskim:mentions | umls-concept:C0919437 | lld:lifeskim |
| pubmed-article:17517630 | lifeskim:mentions | umls-concept:C1880274 | lld:lifeskim |
| pubmed-article:17517630 | lifeskim:mentions | umls-concept:C0168424 | lld:lifeskim |
| pubmed-article:17517630 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:17517630 | lifeskim:mentions | umls-concept:C1537044 | lld:lifeskim |
| pubmed-article:17517630 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:17517630 | lifeskim:mentions | umls-concept:C0392337 | lld:lifeskim |
| pubmed-article:17517630 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:17517630 | lifeskim:mentions | umls-concept:C1553877 | lld:lifeskim |
| pubmed-article:17517630 | lifeskim:mentions | umls-concept:C1608885 | lld:lifeskim |
| pubmed-article:17517630 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:17517630 | pubmed:dateCreated | 2007-5-23 | lld:pubmed |
| pubmed-article:17517630 | pubmed:abstractText | The three deleted in liver cancer genes (DLC1-3) encode Rho-GTPase-activating proteins (RhoGAPs) whose expression is frequently down-regulated or silenced in a variety of human malignancies. The RhoGAP activity is required for full DLC-dependent tumor suppressor activity. Here we report that DLC1 and DLC3 bind to human tensin1 and its chicken homolog. The binding has been mapped to the tensin Src homology 2 (SH2) and phosphotyrosine binding (PTB) domains at the C terminus of tensin proteins. Distinct DLC1 sequences are required for SH2 and PTB binding. DCL binding to both domains is constitutive under basal conditions. The SH2 binding depends on a tyrosine in DCL1 (Y442) but is phosphotyrosine-independent, a highly unusual feature for SH2 binding. DLC1 competed with the binding of other proteins to the tensin C terminus, including beta 3-integrin binding to the PTB domain. Point mutation of a critical tyrosine residue (Y442F) in DLC1 rendered the protein deficient for binding the tensin SH2 domain and binding full-length tensin. The Y442F protein was diffusely cytoplasmic, in contrast to the localization of wild-type DLC1 to focal adhesions, but it retained the ability to reduce the intracellular levels of Rho-GTP. The Y442F mutant displayed markedly reduced biological activity, as did a mutant that was RhoGAP-deficient. The results suggest that DLC1 is a multifunctional protein whose biological activity depends on cooperation between its tensin binding and RhoGAP activities, although neither activity depends on the other. | lld:pubmed |
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| pubmed-article:17517630 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17517630 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17517630 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17517630 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17517630 | pubmed:month | May | lld:pubmed |
| pubmed-article:17517630 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:17517630 | pubmed:author | pubmed-author:PopescuNichol... | lld:pubmed |
| pubmed-article:17517630 | pubmed:author | pubmed-author:YamadaKenneth... | lld:pubmed |
| pubmed-article:17517630 | pubmed:author | pubmed-author:VassWilliam... | lld:pubmed |
| pubmed-article:17517630 | pubmed:author | pubmed-author:LiGuorongG | lld:pubmed |
| pubmed-article:17517630 | pubmed:author | pubmed-author:LowyDouglas... | lld:pubmed |
| pubmed-article:17517630 | pubmed:author | pubmed-author:AsnaghiLauraL | lld:pubmed |
| pubmed-article:17517630 | pubmed:author | pubmed-author:QianXiaolanX | lld:pubmed |
| pubmed-article:17517630 | pubmed:author | pubmed-author:BravermanRich... | lld:pubmed |
| pubmed-article:17517630 | pubmed:author | pubmed-author:AsmussenHolly... | lld:pubmed |
| pubmed-article:17517630 | pubmed:author | pubmed-author:PapageorgeAle... | lld:pubmed |
| pubmed-article:17517630 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17517630 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:17517630 | pubmed:volume | 104 | lld:pubmed |
| pubmed-article:17517630 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17517630 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17517630 | pubmed:pagination | 9012-7 | lld:pubmed |
| pubmed-article:17517630 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:17517630 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17517630 | pubmed:articleTitle | Oncogenic inhibition by a deleted in liver cancer gene requires cooperation between tensin binding and Rho-specific GTPase-activating protein activities. | lld:pubmed |
| pubmed-article:17517630 | pubmed:affiliation | Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA. | lld:pubmed |
| pubmed-article:17517630 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17517630 | pubmed:publicationType | Research Support, N.I.H., Intramural | lld:pubmed |
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